ID   ANM3_ORYSJ              Reviewed;         620 AA.
AC   A3BMN9; Q0D490; Q69R11;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable protein arginine N-methyltransferase 3;
DE            EC=2.1.1.-;
GN   Name=PRMT3; OrderedLocusNames=Os07g0640000, LOC_Os07g44640;
GN   ORFNames=OJ1340_C08.133, OsJ_024311;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-620.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the guanidino
CC       nitrogens of arginyl residues in some proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The zinc-finger is responsible for substrate specificity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Protein arginine N-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD31262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF22333.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP005292; BAD31262.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008213; BAF22333.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000144; EAZ40828.1; -; Genomic_DNA.
DR   EMBL; AK105489; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015647334.1; XM_015791848.1.
DR   AlphaFoldDB; A3BMN9; -.
DR   SMR; A3BMN9; -.
DR   STRING; 4530.OS07T0640000-01; -.
DR   iPTMnet; A3BMN9; -.
DR   PaxDb; A3BMN9; -.
DR   PRIDE; A3BMN9; -.
DR   GeneID; 4344057; -.
DR   KEGG; osa:4344057; -.
DR   eggNOG; KOG1499; Eukaryota.
DR   HOGENOM; CLU_017375_1_2_1; -.
DR   InParanoid; A3BMN9; -.
DR   OrthoDB; 840669at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000007752; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   Genevisible; A3BMN9; OS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016274; F:protein-arginine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0018216; P:peptidyl-arginine methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025799; Arg_MeTrfase.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR11006; PTHR11006; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   Pfam; PF12756; zf-C2H2_2; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS51678; SAM_MT_PRMT; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Methyltransferase; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..620
FT                   /note="Probable protein arginine N-methyltransferase 3"
FT                   /id="PRO_0000293992"
FT   DOMAIN          253..582
FT                   /note="SAM-dependent MTase PRMT-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT   ZN_FING         55..78
FT                   /note="C2H2-type 1"
FT   ZN_FING         110..137
FT                   /note="C2H2-type 2; degenerate"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..44
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   620 AA;  67943 MW;  BDE720333F6F19D1 CRC64;
     MATREHELRP EQERLGEDRE EYEDGEEEEE EGEEGWDDWE SDGDDAGGGG GGGGLLCLFC
     SARFDSESSL FSHCASEHRF DFYRVVKETG MDFYGCIKLI NFVRSKVAEN KCWSCGQVFS
     SNSELCGHLH ALEIPQLEGK VPWGDDVYLK PFLEDDSLLH SLSVFDDDDE DDCGMPMEKG
     GCSAGNGSLA ETCESNLKSI INDGSDVIDR FERTCTIEST DGECSGSLAQ EPSDKQLKIA
     RASAAARGIK SVDESYFGSY SSFGIHREML GDKVRTEAYR DALLGNPSLM NGATVLDVGC
     GTGILSLFAA KAGASRVIAV DGSAKMVSVA TEVAKSNGFL YDENMEMQQK RDTQVITVVH
     TKAEELNHKI QVPSNKFDVL VSEWMGYCLL YESMLSSVLY ARDHFLKPGG AILPDTATIF
     GAGFGKGGTS LPFWENVYGF DMSCIGKEVT GNSARFPVVD ILASEDIVTE TAVLNSFDLA
     TMKENEMDFT SSFELRLSES GVSQSGVTWC YGIILWFDTG FTNRFCKEKP VNLSTSPFST
     PTHWSQTIFT FEEPIAMAKE ESAVVSSASV GTDECPAVMI RSRISIVRAS EHRSIDISIE
     TTGISSDGRK RSWPVQIFNL